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- W2015204889 abstract "Versican belongs to the family of the large aggregating chondroitin sulfate proteoglycans located primarily within the extracellular matrix (ECM). Versican, like other members of its family, has unique N- and C-terminal globular regions, each with multiple motifs. A large glycosaminoglycan-binding region lies between them. This review will begin by outlining these structures, in the context of ECM proteoglycans. The diverse binding partners afforded to versican by virtue of its modular design will then be examined. These include ECM components, such as hyaluronan, type I collagen, tenascin-R, fibulin-1, and -2, fibrillin-1, fibronectin, P- and L-selectins, and chemokines. Versican also binds to the cell surface proteins CD44, integrin β1, epidermal growth factor receptor, and P-selectin glycoprotein ligand-1. These multiple interactors play important roles in cell behaviour, and the roles of versican in modulating such processes are discussed." @default.
- W2015204889 created "2016-06-24" @default.
- W2015204889 creator A5020284848 @default.
- W2015204889 creator A5028932344 @default.
- W2015204889 creator A5032397551 @default.
- W2015204889 creator A5048751010 @default.
- W2015204889 creator A5088884825 @default.
- W2015204889 date "2005-07-01" @default.
- W2015204889 modified "2023-10-15" @default.
- W2015204889 title "The interaction of versican with its binding partners" @default.
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